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Literature summary for 1.1.1.6 extracted from

  • Hoang, H.; Tran, T.; Jung, C.
    The activation of glycerol dehydrogenase from Escherichia coli by ppGpp (2020), Bull. Korean Chem. Soc., 41, 133-138 .
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
ppGpp ppGpp increases GldA activity with the half maximal activation at 33.1 microM Escherichia coli

Application

Application Comment Organism
analysis GldA shows a strong intrinsic fluorescence at 320 nm, when excited at 280 nm. The fluorescence intensity decreases in the presence of NAD+, NADH, and dihydroxyacetone, the substrate and products for GldA, which allows to determine the dissociation constants for those molecules as 110.6 microM, 9,1 microM, 33.3 mM, respectively Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
GDP
-
Escherichia coli
GTP
-
Escherichia coli
Tris(hydroxymethyl)aminomethane competitive with respect to glycerol Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.22
-
NAD+ pH 7.5, 25°C Escherichia coli
48.9
-
glycerol pH 7.5, 25°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9S5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycerol + NAD+
-
Escherichia coli glycerone + NADH + H+
-
?

Synonyms

Synonyms Comment Organism
GldA
-
Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
12
-
-
Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
10.6
-
GDP pH 7.5, 25°C Escherichia coli
16.1
-
GTP pH 7.5, 25°C Escherichia coli